ArticleChemico-biological interactions2015
Development of a high-throughput in vitro assay to identify selective inhibitors for human ALDH1A1.
Article in Chemico-biological interactions, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- A synergistic deep learning and machine learning framework for screening heterocyclic compounds against ALDH1A1.Molecular diversity · 2026Article
- Article
- Donor-PeT Control of Intersystem Crossing Enables ALDH1A1-Activated Photodynamic Therapy.ACS chemical biology · 2026Article
- "Heptadecanol" a phytochemical multi-target inhibitor of SMYD3 & GFPT2 proteins in non-small cell lung cancer: an in-silico & in-vitro investigation.Journal of computer-aided molecular design · 2025Article
- Retinoic acid signaling and metabolism in heart failure.American journal of physiology. Heart and circulatory physiology · 2025Review
- Identification ofMolecules (Basel, Switzerland) · 2025Article
- Development of substituted benzimidazoles as inhibitors of human aldehyde dehydrogenase 1A isoenzymes.Chemico-biological interactions · 2024Article
- Scaffold hopping based designing of selective ALDH1A1 inhibitors to overcome cyclophosphamide resistance: synthesis and biological evaluation.RSC medicinal chemistry · 2024Article
- A simple method for developing lysine targeted covalent protein reagents.Nature communications · 2023Article
- ALDEFLUOR activity, ALDH isoforms, and their clinical significance in cancers.Journal of enzyme inhibition and medicinal chemistry · 2023Article
- Modification of lysine-260 2-hydroxyisobutyrylation destabilizes ALDH1A1 expression to regulate bladder cancer progression.iScience · 2023Article
- High-resolution structural-omics of human liver enzymes.Cell reports · 2023Article
- A cryo-electron microscopic approach to elucidate protein structures from human brain microsomes.Life science alliance · 2023Article
- Simultaneous solving high-resolution structures of various enzymes from human kidney microsomes.Life science alliance · 2023Article
- A Novel ALDH1A1 Inhibitor Blocks Platinum-Induced Senescence and Stemness in Ovarian Cancer.Cancers · 2022Article
- Cryo-EM structure of the fatty acid reductase LuxC-LuxE complex provides insights into bacterial bioluminescence.The Journal of biological chemistry · 2022Article
- A prodrug strategy for theRSC chemical biology · 2022Article
- An EHMT2/NFYA-ALDH2 signaling axis modulates the RAF pathway to regulate paclitaxel resistance in lung cancer.Molecular cancer · 2022Article
- Structural and biochemical evidence that ATP inhibits the cancer biomarker human aldehyde dehydrogenase 1A3.Communications biology · 2022Article
- Computer-Aided Drug Design (CADD) to De-Orphanize Marine Molecules: Finding Potential Therapeutic Agents for Neurodegenerative and Cardiovascular Diseases.Marine drugs · 2022Article
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2 authors.
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Abstract
The human aldehyde dehydrogenase (ALDH) superfamily consists of at least 19 enzymes that metabolize endogenous and exogenous aldehydes. Currently, there are no commercially available inhibitors that target ALDH1A1 but have little to no effect on the structurally and functionally similar ALDH2. Here we present the first human ALDH1A1 structure, as the apo-enzyme and in complex with its cofactor NADH to a resolution of 1.75 and 2.1Å, respectfully. Structural comparisons of the cofactor binding sites in ALDH1A1 with other closely related ALDH enzymes illustrate a high degree of similarity. In order to minimize discovery of compounds that inhibit both isoenzymes by interfering with their conserved cofactor binding sites, this study reports the use of an in vitro, NAD(+)-independent, esterase-based high-throughput screen (HTS) of 64,000 compounds to discover novel, selective inhibitors of ALDH1A1. We describe 256 hits that alter the esterase activity of ALDH1A1. The effects on aldehyde oxidation of 67 compounds were further analyzed, with 30 selectively inhibiting ALDH1A1 compared to ALDH2 and ALDH3A1. One compound inhibited ALDH1A1 and ALDH2, while another inhibited ALDH1A1, ALDH2, and the more distantly related ALDH3A1. The results presented here indicate that this in vitro enzyme activity screening protocol successfully identified ALDH1A1 inhibitors with a high degree of isoenzyme selectivity. The compounds identified via this screen plus the screening methodology itself represent a starting point for the development of highly potent and selective inhibitors of ALDH1A1 that may be utilized to better understand the role of this enzyme in both normal and disease states.
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